Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D001105:Archaea / Q000737:chemistry*; D018833:Chaperonins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D019281:Dimerization; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D009154:Mutation; D011487:Protein Conformation / Q000187:drug effects; D017510:Protein Folding; D020673:Protein Renaturation; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry; D019712:Thermococcus / Q000737:chemistry
D018832:Molecular Chaperones; D021122:Protein Subunits; D000255:Adenosine Triphosphate; D018833:Chaperonins